Relationships between the orientation and the structural properties of peptides and their membrane interactions
| Autor: | Laurence Lins, Marc Decaffmeyer, Annick Thomas, Robert Brasseur |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Lipid organization
Models Molecular Tilted peptide Membrane Fluidity Stereochemistry Recombinant Fusion Proteins Membrane lipids Molecular Sequence Data Retroviridae Proteins Biophysics Galanin Wasp Venoms Peptide Membrane Fusion Biochemistry Biophysical Phenomena Membrane Lipids Membrane Microdomains Fusion peptide Membrane fluidity Animals Humans Amino Acid Sequence Conformation chemistry.chemical_classification Chemistry Bilayer Peripheral membrane protein Membrane Proteins Lipid bilayer fusion Biological membrane Cell Biology Membrane protein Thermodynamics Peptides Hydrophobic and Hydrophilic Interactions CPP |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1778:1537-1544 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2008.04.006 |
| Popis: | Physical properties of membranes, such as fluidity, charge or curvature influence their function. Proteins and peptides can modulate those properties and conversely, the lipids can affect the activity and/or the structure of the former. Tilted peptides are short hydrophobic protein fragments characterized by an asymmetric distribution of their hydrophobic residues when helical. They were detected in viral fusion proteins and in proteins involved in different biological processes that need membrane destabilization. Those peptides and non lamellar lipids such as PE or PA appear to cooperate in the lipid destabilization process by enhancing the formation of negatively-curved domains. Such highly bent lipidic structures could favour the formation of the viral fusion pore intermediates or that of toroidal pores. Structural flexibility appears as another crucial property for the interaction of peptides with membranes. Computational analysis on another kind of lipid-interacting peptides, i.e. cell penetrating peptides (CPP) suggests that peptides being conformationally polymorphic should be more prone to traverse the bilayer. Future investigations on the structural intrinsic properties of tilted peptides and the influence of CPP on the bilayer organization using the techniques described in this chapter should help to further understand the molecular determinants of the peptide/lipid inter-relationships. |
| Databáze: | OpenAIRE |
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